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This review serves to highlight the role of protein glycosylation in Alzheimer disease (<jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content>), a topic that has not been thoroughly investigated, although glycosylation defects have been observed in <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> patients. The major pathological hallmarks in <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> are neurofibrillary tangles and amyloid plaques. Neurofibrillary tangles are composed of phosphorylated tau, and the plaques are composed of amyloid \u03b2\u2010peptide (A\u03b2), which is generated from amyloid precursor protein (<jats:styled-content style=\"fixed-case\">APP<\/jats:styled-content>). Defects in glycosylation of <jats:styled-content style=\"fixed-case\">APP<\/jats:styled-content>, tau and other proteins have been reported in <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content>. Another interesting observation is that the two proteases required for the generation of amyloid \u03b2\u2010peptide (A\u03b2), i.e. \u03b3\u2010secretase and \u03b2\u2010secretase, also have roles in protein glycosylation. For instance, \u03b3\u2010secretase and \u03b2\u2010secretase affect the extent of complex N\u2010glycosylation and sialylation of <jats:styled-content style=\"fixed-case\">APP<\/jats:styled-content>, respectively. These processes may be important in <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> pathogenesis, as proper intracellular sorting, processing and export of <jats:styled-content style=\"fixed-case\">APP<\/jats:styled-content> are affected by how it is glycosylated. Furthermore, lack of one of the key components of \u03b3\u2010secretase, presenilin, leads to defective glycosylation of many additional proteins that are related to <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> pathogenesis and\/or neuronal function, including nicastrin, reelin, butyrylcholinesterase, cholinesterase, neural cell adhesion molecule, v\u2010<jats:styled-content style=\"fixed-case\">ATP<\/jats:styled-content>ase, and tyrosine\u2010related kinase\u00a0B. Improved understanding of the effects of <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> on protein glycosylation, and vice\u00a0versa, may therefore be important for improving the diagnosis and treatment of <jats:styled-content style=\"fixed-case\">AD<\/jats:styled-content> patients.<\/jats:p>","DOI":"10.1111\/febs.12590","type":"journal-article","created":{"date-parts":[[2013,10,30]],"date-time":"2013-10-30T13:59:25Z","timestamp":1383141565000},"page":"46-62","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":298,"title":["The role of protein glycosylation in Alzheimer disease"],"prefix":"10.1111","volume":"281","author":[{"given":"Sophia","family":"Schedin\u2010Weiss","sequence":"first","affiliation":[{"name":"Karolinska Institutet Alzheimer Disease Research Center (KI\u2010ADRC) Novum Stockholm 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